Distinct isocomplexes of the TRAPP trafficking factor coexist inside human cells.
The transport protein particle (TRAPP) complex is required for proper vesicular transport from the ER to the Golgi. The composition of yeast TRAPP is well characterized, but the organization of mammalian TRAPP complex remains elusive. Using a tandem affinity purification (TAP) approach, we provide first experimental proof for the association of NIBP (NIK/IKKbeta binding protein) with Bet3 and find two human paralogs of Trs33 (A and B) associated with Bet3. Interaction studies and gel filtration analysis reveal that both proteins are part of human TRAPP and might mark two distinct isocomplexes that exert different functions in the regulation of ER-to-Golgi traffic.
Kümmel
Daniel
D
Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strabetae 10, 13125 Berlin, Germany.
Oeckinghaus
Andrea
A
Wang
Chengcheng
C
Krappmann
Daniel
D
Heinemann
Udo
U
D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000378:metabolism; D002460:Cell Line; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism*; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D021381:Protein Transport; D033921:Vesicular Transport Proteins / Q000235:genetics / Q000378:metabolism*
D002352:Carrier Proteins; D036341:Intercellular Signaling Peptides and Proteins; C503571:TRAPPC3 protein, human; C534009:TRAPPC6A protein, human; C503887:TRAPPC9 protein, human; D033921:Vesicular Transport Proteins; C406327:transport protein particle, TRAPP